LinkDB: 6DZO
Original site: 6DZO
Chemical substance (6) PDB-CCD (6) Chemical reaction (1) KEGG ENZYME (1) Gene (2) KEGG GENES (2) Protein sequence (6) UniProt (2) SWISS-PROT (2) PDBSTR (2) Protein domain (11) InterPro (9) PROSITE (2) All databases (26)
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HEADER LYASE/LYASE INHIBITOR 05-JUL-18 6DZO
TITLE CRYSTAL STRUCTURE OF SALMONELLA TYPHIMURIUM TRYPTOPHAN SYNTHASE MUTANT
TITLE 2 BETA-Q114A WITH 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL
TITLE 3 DIHYDROGEN PHOSPHATE (F9F) AT THE ALPHA-SITE, CESIUM ION AT THE METAL
TITLE 4 COORDINATION SITE, AND (E)-N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
TITLE 5 METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-SERINE AT THE BETA-SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPTOPHAN SYNTHASE ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.1.20;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TRYPTOPHAN SYNTHASE BETA CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 EC: 4.2.1.20;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM (STRAIN LT2 / SGSC1412 /
SOURCE 3 ATCC 700720);
SOURCE 4 ORGANISM_TAXID: 99287;
SOURCE 5 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 6 GENE: TRPA, STM1727;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEBA-10 BETA-Q114A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM (STRAIN LT2 / SGSC1412 /
SOURCE 13 ATCC 700720);
SOURCE 14 ORGANISM_TAXID: 99287;
SOURCE 15 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 16 GENE: TRPB, STM1726;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PEBA-10 BETA-Q114A
KEYWDS Q114A, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.HILARIO,M.F.DUNN,L.J.MUELLER,L.FAN
REVDAT 4 11-OCT-23 6DZO 1 REMARK
REVDAT 3 06-MAY-20 6DZO 1 TITLE JRNL
REVDAT 2 18-DEC-19 6DZO 1 REMARK
REVDAT 1 10-JUL-19 6DZO 0
JRNL AUTH E.HILARIO,M.F.DUNN,L.J.MUELLER,L.FAN
JRNL TITL CRYSTAL STRUCTURE OF SALMONELLA TYPHIMURIUM TRYPTOPHAN
JRNL TITL 2 SYNTHASE MUTANT BETA-Q114A WITH
JRNL TITL 3 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL
JRNL TITL 4 DIHYDROGEN PHOSPHATE (F9F) AT THE ALPHA-SITE, CESIUM ION AT
JRNL TITL 5 THE METAL COORDINATION SITE, AND
JRNL TITL 6 (E)-N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
JRNL TITL 7 METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-SERINE AT THE BETA-SITE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 76612
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3982
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4986
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 99
REMARK 3 SOLVENT ATOMS : 684
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.099
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.093
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6DZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235488.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80656
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.13100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, DM 7.0.059
REMARK 200 STARTING MODEL: 4HPX
REMARK 200
REMARK 200 REMARK: LARGE PLATE-LIKE CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM BICINE-CSOH PH 7.8, 50MM CESIUM
REMARK 280 CHLORIDE, 9% PEG 8,000, 2MM SPERMINE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 90.67450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.19000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 90.67450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.19000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -324.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 392 CG CD CE NZ
REMARK 470 ARG B 394 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG B 222 O HOH B 501 2.08
REMARK 500 O HOH A 524 O HOH B 519 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 15 64.85 32.45
REMARK 500 ALA A 190 49.11 -108.03
REMARK 500 PHE A 212 117.32 101.02
REMARK 500 THR B 165 -156.21 -131.11
REMARK 500 SER B 308 -150.90 -136.00
REMARK 500 ARG B 394 -122.09 -106.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 914 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 915 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 916 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B 917 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH B 918 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH B 919 DISTANCE = 7.27 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 401 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 66 O
REMARK 620 2 THR B 66 OG1 58.3
REMARK 620 3 THR B 69 O 70.4 122.6
REMARK 620 4 THR B 71 O 84.2 62.4 90.0
REMARK 620 5 HOH B 647 O 80.9 60.3 136.0 120.0
REMARK 620 6 HOH B 801 O 136.8 132.2 73.0 73.7 142.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 403 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 231 O
REMARK 620 2 GLY B 232 O 71.4
REMARK 620 3 GLU B 256 OE2 112.6 161.1
REMARK 620 4 GLY B 268 O 95.5 121.0 77.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 403 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 232 O
REMARK 620 2 PHE B 306 O 101.7
REMARK 620 3 SER B 308 O 86.8 76.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 403 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 232 O
REMARK 620 2 GLY B 268 O 154.0
REMARK 620 3 LEU B 304 O 107.8 91.6
REMARK 620 4 PHE B 306 O 78.1 121.5 85.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F9F A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KOU B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 418
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HN4 RELATED DB: PDB
REMARK 900 AMINOACRYLATE
REMARK 900 RELATED ID: 4HPX RELATED DB: PDB
REMARK 900 AMINOACRYLATE
REMARK 900 RELATED ID: 6DZ4 RELATED DB: PDB
REMARK 900 PLS
DBREF 6DZO A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 6DZO B 2 395 UNP P0A2K1 TRPB_SALTY 2 395
SEQADV 6DZO ALA B 114 UNP P0A2K1 GLN 114 ENGINEERED MUTATION
SEQRES 1 A 268 MET GLU ARG TYR GLU ASN LEU PHE ALA GLN LEU ASN ASP
SEQRES 2 A 268 ARG ARG GLU GLY ALA PHE VAL PRO PHE VAL THR LEU GLY
SEQRES 3 A 268 ASP PRO GLY ILE GLU GLN SER LEU LYS ILE ILE ASP THR
SEQRES 4 A 268 LEU ILE ASP ALA GLY ALA ASP ALA LEU GLU LEU GLY VAL
SEQRES 5 A 268 PRO PHE SER ASP PRO LEU ALA ASP GLY PRO THR ILE GLN
SEQRES 6 A 268 ASN ALA ASN LEU ARG ALA PHE ALA ALA GLY VAL THR PRO
SEQRES 7 A 268 ALA GLN CYS PHE GLU MET LEU ALA LEU ILE ARG GLU LYS
SEQRES 8 A 268 HIS PRO THR ILE PRO ILE GLY LEU LEU MET TYR ALA ASN
SEQRES 9 A 268 LEU VAL PHE ASN ASN GLY ILE ASP ALA PHE TYR ALA ARG
SEQRES 10 A 268 CYS GLU GLN VAL GLY VAL ASP SER VAL LEU VAL ALA ASP
SEQRES 11 A 268 VAL PRO VAL GLU GLU SER ALA PRO PHE ARG GLN ALA ALA
SEQRES 12 A 268 LEU ARG HIS ASN ILE ALA PRO ILE PHE ILE CYS PRO PRO
SEQRES 13 A 268 ASN ALA ASP ASP ASP LEU LEU ARG GLN VAL ALA SER TYR
SEQRES 14 A 268 GLY ARG GLY TYR THR TYR LEU LEU SER ARG SER GLY VAL
SEQRES 15 A 268 THR GLY ALA GLU ASN ARG GLY ALA LEU PRO LEU HIS HIS
SEQRES 16 A 268 LEU ILE GLU LYS LEU LYS GLU TYR HIS ALA ALA PRO ALA
SEQRES 17 A 268 LEU GLN GLY PHE GLY ILE SER SER PRO GLU GLN VAL SER
SEQRES 18 A 268 ALA ALA VAL ARG ALA GLY ALA ALA GLY ALA ILE SER GLY
SEQRES 19 A 268 SER ALA ILE VAL LYS ILE ILE GLU LYS ASN LEU ALA SER
SEQRES 20 A 268 PRO LYS GLN MET LEU ALA GLU LEU ARG SER PHE VAL SER
SEQRES 21 A 268 ALA MET LYS ALA ALA SER ARG ALA
SEQRES 1 B 394 THR THR LEU LEU ASN PRO TYR PHE GLY GLU PHE GLY GLY
SEQRES 2 B 394 MET TYR VAL PRO GLN ILE LEU MET PRO ALA LEU ASN GLN
SEQRES 3 B 394 LEU GLU GLU ALA PHE VAL SER ALA GLN LYS ASP PRO GLU
SEQRES 4 B 394 PHE GLN ALA GLN PHE ALA ASP LEU LEU LYS ASN TYR ALA
SEQRES 5 B 394 GLY ARG PRO THR ALA LEU THR LYS CYS GLN ASN ILE THR
SEQRES 6 B 394 ALA GLY THR ARG THR THR LEU TYR LEU LYS ARG GLU ASP
SEQRES 7 B 394 LEU LEU HIS GLY GLY ALA HIS LYS THR ASN GLN VAL LEU
SEQRES 8 B 394 GLY GLN ALA LEU LEU ALA LYS ARG MET GLY LYS SER GLU
SEQRES 9 B 394 ILE ILE ALA GLU THR GLY ALA GLY ALA HIS GLY VAL ALA
SEQRES 10 B 394 SER ALA LEU ALA SER ALA LEU LEU GLY LEU LYS CYS ARG
SEQRES 11 B 394 ILE TYR MET GLY ALA LYS ASP VAL GLU ARG GLN SER PRO
SEQRES 12 B 394 ASN VAL PHE ARG MET ARG LEU MET GLY ALA GLU VAL ILE
SEQRES 13 B 394 PRO VAL HIS SER GLY SER ALA THR LEU LYS ASP ALA CYS
SEQRES 14 B 394 ASN GLU ALA LEU ARG ASP TRP SER GLY SER TYR GLU THR
SEQRES 15 B 394 ALA HIS TYR MET LEU GLY THR ALA ALA GLY PRO HIS PRO
SEQRES 16 B 394 TYR PRO THR ILE VAL ARG GLU PHE GLN ARG MET ILE GLY
SEQRES 17 B 394 GLU GLU THR LYS ALA GLN ILE LEU ASP LYS GLU GLY ARG
SEQRES 18 B 394 LEU PRO ASP ALA VAL ILE ALA CYS VAL GLY GLY GLY SER
SEQRES 19 B 394 ASN ALA ILE GLY MET PHE ALA ASP PHE ILE ASN ASP THR
SEQRES 20 B 394 SER VAL GLY LEU ILE GLY VAL GLU PRO GLY GLY HIS GLY
SEQRES 21 B 394 ILE GLU THR GLY GLU HIS GLY ALA PRO LEU LYS HIS GLY
SEQRES 22 B 394 ARG VAL GLY ILE TYR PHE GLY MET LYS ALA PRO MET MET
SEQRES 23 B 394 GLN THR ALA ASP GLY GLN ILE GLU GLU SER TYR SER ILE
SEQRES 24 B 394 SER ALA GLY LEU ASP PHE PRO SER VAL GLY PRO GLN HIS
SEQRES 25 B 394 ALA TYR LEU ASN SER ILE GLY ARG ALA ASP TYR VAL SER
SEQRES 26 B 394 ILE THR ASP ASP GLU ALA LEU GLU ALA PHE LYS THR LEU
SEQRES 27 B 394 CYS ARG HIS GLU GLY ILE ILE PRO ALA LEU GLU SER SER
SEQRES 28 B 394 HIS ALA LEU ALA HIS ALA LEU LYS MET MET ARG GLU GLN
SEQRES 29 B 394 PRO GLU LYS GLU GLN LEU LEU VAL VAL ASN LEU SER GLY
SEQRES 30 B 394 ARG GLY ASP LYS ASP ILE PHE THR VAL HIS ASP ILE LEU
SEQRES 31 B 394 LYS ALA ARG GLY
HET F9F A 301 22
HET DMS A 302 4
HET DMS A 303 4
HET DMS A 304 4
HET DMS A 305 4
HET DMS A 306 4
HET CL A 307 1
HET CL A 308 1
HET CL A 309 1
HET CS B 401 1
HET EDO B 402 4
HET CS B 403 3
HET DMS B 404 4
HET DMS B 405 4
HET DMS B 406 4
HET DMS B 407 4
HET KOU B 408 22
HET CL B 409 1
HET CL B 410 1
HET CL B 411 1
HET CL B 412 1
HET CL B 413 1
HET CL B 414 1
HET CL B 415 1
HET CL B 416 1
HET CL B 417 1
HET CL B 418 1
HETNAM F9F 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL
HETNAM 2 F9F DIHYDROGEN PHOSPHATE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM CL CHLORIDE ION
HETNAM CS CESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM KOU (E)-N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
HETNAM 2 KOU METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-SERINE
HETSYN F9F N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-
HETSYN 2 F9F ETHYLPHOSPHATE, F9
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 F9F C9 H11 F3 N O7 P S
FORMUL 4 DMS 9(C2 H6 O S)
FORMUL 9 CL 13(CL 1-)
FORMUL 12 CS 2(CS 1+)
FORMUL 13 EDO C2 H6 O2
FORMUL 19 KOU C11 H15 N2 O8 P
FORMUL 30 HOH *684(H2 O)
HELIX 1 AA1 MET A 1 ARG A 14 1 14
HELIX 2 AA2 GLY A 29 ALA A 43 1 15
HELIX 3 AA3 GLY A 61 ALA A 74 1 14
HELIX 4 AA4 THR A 77 HIS A 92 1 16
HELIX 5 AA5 TYR A 102 ASN A 108 1 7
HELIX 6 AA6 GLY A 110 GLY A 122 1 13
HELIX 7 AA7 PRO A 132 GLU A 135 5 4
HELIX 8 AA8 SER A 136 HIS A 146 1 11
HELIX 9 AA9 ASP A 159 GLY A 170 1 12
HELIX 10 AB1 LEU A 193 TYR A 203 1 11
HELIX 11 AB2 SER A 216 ALA A 226 1 11
HELIX 12 AB3 GLY A 234 ASN A 244 1 11
HELIX 13 AB4 SER A 247 ALA A 265 1 19
HELIX 14 AB5 PRO B 18 ILE B 20 5 3
HELIX 15 AB6 LEU B 21 LYS B 37 1 17
HELIX 16 AB7 ASP B 38 TYR B 52 1 15
HELIX 17 AB8 ASP B 79 LEU B 81 5 3
HELIX 18 AB9 LYS B 87 MET B 101 1 15
HELIX 19 AC1 GLY B 113 GLY B 127 1 15
HELIX 20 AC2 ALA B 136 GLN B 142 1 7
HELIX 21 AC3 GLN B 142 MET B 152 1 11
HELIX 22 AC4 THR B 165 TYR B 181 1 17
HELIX 23 AC5 PRO B 196 PHE B 204 1 9
HELIX 24 AC6 ARG B 206 GLY B 221 1 16
HELIX 25 AC7 GLY B 234 ALA B 242 1 9
HELIX 26 AC8 ASP B 243 ILE B 245 5 3
HELIX 27 AC9 GLY B 261 GLY B 265 5 5
HELIX 28 AD1 ALA B 269 GLY B 274 1 6
HELIX 29 AD2 SER B 301 ASP B 305 5 5
HELIX 30 AD3 GLY B 310 ILE B 319 1 10
HELIX 31 AD4 ASP B 329 GLY B 344 1 16
HELIX 32 AD5 ALA B 348 GLN B 365 1 18
HELIX 33 AD6 GLY B 380 LYS B 382 5 3
HELIX 34 AD7 ASP B 383 ARG B 394 1 12
SHEET 1 AA1 9 ALA A 149 PRO A 150 0
SHEET 2 AA1 9 SER A 125 VAL A 128 1 N VAL A 126 O ALA A 149
SHEET 3 AA1 9 ILE A 97 MET A 101 1 N MET A 101 O LEU A 127
SHEET 4 AA1 9 LEU A 48 GLY A 51 1 N LEU A 50 O GLY A 98
SHEET 5 AA1 9 ALA A 18 THR A 24 1 N VAL A 23 O GLY A 51
SHEET 6 AA1 9 GLY A 230 SER A 233 1 O ALA A 231 N VAL A 20
SHEET 7 AA1 9 ALA A 208 GLY A 211 1 N GLN A 210 O ILE A 232
SHEET 8 AA1 9 THR A 174 LEU A 177 1 N LEU A 176 O LEU A 209
SHEET 9 AA1 9 ILE A 153 CYS A 154 1 N CYS A 154 O TYR A 175
SHEET 1 AA2 4 TYR B 8 PHE B 9 0
SHEET 2 AA2 4 PHE B 12 TYR B 16 -1 O PHE B 12 N PHE B 9
SHEET 3 AA2 4 GLY B 281 MET B 286 -1 O LYS B 283 N GLY B 13
SHEET 4 AA2 4 ARG B 275 TYR B 279 -1 N ARG B 275 O MET B 286
SHEET 1 AA3 6 LEU B 59 LYS B 61 0
SHEET 2 AA3 6 THR B 71 ARG B 77 -1 O LEU B 75 N THR B 60
SHEET 3 AA3 6 GLN B 370 LEU B 376 1 O LEU B 372 N THR B 72
SHEET 4 AA3 6 ALA B 226 CYS B 230 1 N ILE B 228 O ASN B 375
SHEET 5 AA3 6 GLY B 251 GLY B 259 1 O ILE B 253 N VAL B 227
SHEET 6 AA3 6 ASP B 323 THR B 328 1 O ILE B 327 N GLY B 258
SHEET 1 AA4 4 GLU B 155 VAL B 159 0
SHEET 2 AA4 4 LYS B 129 GLY B 135 1 N ILE B 132 O ILE B 157
SHEET 3 AA4 4 GLU B 105 GLU B 109 1 N ALA B 108 O TYR B 133
SHEET 4 AA4 4 ALA B 184 TYR B 186 1 O HIS B 185 N GLU B 105
LINK O THR B 66 CS CS B 401 1555 1555 3.31
LINK OG1 THR B 66 CS CS B 401 1555 1555 3.41
LINK O THR B 69 CS CS B 401 1555 1555 3.05
LINK O THR B 71 CS CS B 401 1555 1555 3.00
LINK O VAL B 231 CS A CS B 403 1555 1555 3.21
LINK O GLY B 232 CS B CS B 403 1555 1555 2.32
LINK O GLY B 232 CS A CS B 403 1555 1555 3.11
LINK O GLY B 232 CS C CS B 403 1555 1555 2.90
LINK OE2 GLU B 256 CS A CS B 403 1555 1555 2.97
LINK O GLY B 268 CS A CS B 403 1555 1555 3.46
LINK O GLY B 268 CS C CS B 403 1555 1555 2.98
LINK O LEU B 304 CS C CS B 403 1555 1555 3.49
LINK O PHE B 306 CS B CS B 403 1555 1555 2.48
LINK O PHE B 306 CS C CS B 403 1555 1555 3.02
LINK O SER B 308 CS B CS B 403 1555 1555 2.60
LINK CS CS B 401 O HOH B 647 1555 1555 3.18
LINK CS CS B 401 O HOH B 801 1555 1555 2.92
CISPEP 1 ASP A 27 PRO A 28 0 9.71
CISPEP 2 ARG B 55 PRO B 56 0 -1.30
CISPEP 3 HIS B 195 PRO B 196 0 10.57
SITE 1 AC1 20 PHE A 22 GLU A 49 ALA A 59 ILE A 64
SITE 2 AC1 20 LEU A 100 LEU A 127 ALA A 129 ILE A 153
SITE 3 AC1 20 TYR A 175 THR A 183 GLY A 184 PHE A 212
SITE 4 AC1 20 GLY A 213 ILE A 232 GLY A 234 SER A 235
SITE 5 AC1 20 HOH A 412 HOH A 432 HOH A 483 PRO B 18
SITE 1 AC2 6 PHE A 139 ARG A 140 PRO A 150 ILE A 151
SITE 2 AC2 6 PHE A 152 HOH A 417
SITE 1 AC3 8 MET A 1 GLU A 2 ARG A 3 GLU A 119
SITE 2 AC3 8 VAL A 123 ASP A 124 HIS A 146 ASN A 147
SITE 1 AC4 4 LEU A 191 LEU A 193 GLN A 210 ALA A 222
SITE 1 AC5 6 SER A 221 ARG A 225 ALA A 268 HOH A 515
SITE 2 AC5 6 LYS B 99 HOH B 691
SITE 1 AC6 5 ILE A 41 HIS A 92 PRO A 93 THR A 94
SITE 2 AC6 5 ILE A 95
SITE 1 AC7 3 ALA A 167 GLY A 170 HIS A 204
SITE 1 AC8 1 HOH A 597
SITE 1 AC9 4 THR B 66 THR B 69 THR B 71 HOH B 801
SITE 1 AD1 4 GLN B 36 GLN B 42 DMS B 406 HOH B 596
SITE 1 AD2 8 VAL B 231 GLY B 232 GLU B 256 GLY B 268
SITE 2 AD2 8 PRO B 270 LEU B 304 PHE B 306 SER B 308
SITE 1 AD3 4 GLN B 42 PHE B 45 ALA B 46 HOH B 844
SITE 1 AD4 3 ILE B 262 HIS B 267 HIS B 273
SITE 1 AD5 5 GLN B 36 LYS B 37 PRO B 39 GLN B 42
SITE 2 AD5 5 EDO B 402
SITE 1 AD6 4 LYS B 50 ARG B 55 PRO B 56 THR B 57
SITE 1 AD7 22 HIS B 86 LYS B 87 THR B 110 GLY B 111
SITE 2 AD7 22 ALA B 112 GLY B 113 ALA B 114 HIS B 115
SITE 3 AD7 22 THR B 190 GLY B 232 GLY B 233 GLY B 234
SITE 4 AD7 22 SER B 235 ASN B 236 GLY B 303 ASP B 305
SITE 5 AD7 22 GLU B 350 SER B 377 HOH B 540 HOH B 648
SITE 6 AD7 22 HOH B 667 HOH B 743
SITE 1 AD8 3 LEU B 4 LEU B 5 ASN B 6
SITE 1 AD9 3 HOH B 583 HOH B 703 HOH B 887
SITE 1 AE1 3 SER B 297 SER B 299 HOH B 846
SITE 1 AE2 1 HOH B 766
SITE 1 AE3 3 ASP B 225 LYS B 368 HOH B 564
SITE 1 AE4 1 GLY B 179
CRYST1 181.349 58.380 67.300 90.00 94.89 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005514 0.000000 0.000472 0.00000
SCALE2 0.000000 0.017129 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014913 0.00000
(ATOM LINES ARE NOT SHOWN.)
END